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Figure 2
Structural comparison between maMltG and its isoforms from different species. (a) Pairwise structural superimposition of abYdjH (green) with (a) lmMltG (magenta; PDB entry 4iiw) and (b) ecMltG (yellow; PDB entry 2r1f). (c) Graphic representation of maMltG colored relative to the amino-acid sequence conservation degree generated by the ConSurf server. (d) Sequence alignment with structural homologs from different species. Residue Glu307, expected to play a crucial role in LT function as a nucleophile, is indicated by an asterisk (*). Residues that might be involved in the formation of the putative substrate binding site in the catalytic domain are indicated by a hash (#). Completely and partially conserved residues are shown in red and blue, respectively.

IUCrJ
Volume 11| Part 6| November 2024| Pages 903-909
ISSN: 2052-2525